fromAlcaligenes sp. Triacylglycerol lipase EC 3.1.1.3 |
| Lipase QLM shows a wide specificity and high activity towards a variety of esters, and is applicable to enantioselective hydrolysis or esterification of racemic compounds. Lipase QLM is highly active and stable in organic solvents and suitable for synthesis of esters and transesterification |
| Appearance | Beige powder | |
| Activity | ca. 60,000 U/g powder | |
| Molecular weight | 31,000 (SDS-PAGE) | |
| Isoelectric point | 4.9 | |
| Optimum pH | 7 - 9 | |
| pH stability | 6 - 10 | |
| Optimum temperature | 65 - 70 ºC | |
| Thermal stability | Below 50 ºC | |
| Inhibitors | Cationic detergents | |
| Activators | Nonionic detergents | |
| Specificities | Positional specificity | preferentially hydrolyzing the sn-1 and sn-3 positions of triacylglycerols, but non-specific in transesterification reaction |
| Activity on esters | ca. 12,800 U/g (p-Nitrophenyl acetate as a substrate) | |
| Storage | Desiccate and store below 25 ºC | |
| Lipase QLC and QLG are immobilized enzymes designed for various reactions in organic solvents or with no solvents. Lipase QLC is produced by immobilizing Lipase QLM on diatomaceous earth, while Lipase QLG is prepared by immobilizing the same enzyme on granulated diatomaceous earth. Lipase QLC and QLG are applicable to synthesis of optically active substances in organic solvents and transesterification of fats and oils with no solvents. |
| Activity | ca. 20,000 U/g |
| Loss on drying | 1 % or less |
| Storage | Desiccate and store below 25 ºC |
| *1 : Activity of immobilized lipases is expressed as the hydrolytic activity adsorbed on the support materials. |